HydF as a scaffold protein in [FeFe] hydrogenase H-cluster biosynthesis

被引：98

作者：

McGlynn, Shawn E. ^{[1
]}

Shepard, Eric M. ^{[1
]}

Winslow, Mark A. ^{[1
]}

Naumov, Anatoll V. ^{[1
]}

Duschene, Kaitlin S. ^{[1
]}

Posewitz, Matthew C. ^{[2
,3
]}

Broderick, William E. ^{[1
]}

Broderick, Joan B. ^{[1
]}

Peters, John W. ^{[1
]}

机构：

[1] Montana State Univ, Astrobiol Biogeocatalysis Res Ctr, Dept Chem & Biochem, Bozeman, MT 59717 USA

[2] Colorado Sch Mines, Dept Chem & Geochem, Golden, CO 80401 USA

[3] Natl Renewable Energy Lab, Golden, CO 80401 USA

来源：

FEBS LETTERS | 2008年 / 582卷 / 15期

关键词：

hydrogenase; metalloenzyme; iron-sulfur cluster maturation; H-cluster; scaffold;

D O I：

10.1016/j.febslet.2008.04.063

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

In an effort to determine the specific protein component(s) responsible for in vitro activation of the [FeFe] hydrogenase (HydA), the individual maturation proteins HydE, HydF, and HydG from Clostridium acetobutylicum were purified from heterologous expressions in Escherichia coli. Our results demonstrate that HydF isolated from a strain expressing all three maturation proteins is sufficient to confer hydrogenase activity to purified inactive heterologously expressed HydA (expressed in the absence of HydE, HydF, and HydG). These results represent the first in vitro maturation of [FeFe] hydrogenase with purified proteins, and suggest that HydF functions as a scaffold upon which an H-cluster intermediate is synthesized. (C) 2008 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

引用

页码：2183 / 2187

页数：5

共 17 条

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